|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
1-408 |
0e+00 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 679.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 1 MRRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHGMPDLVLEDHVDKRDLRFMGAGAAYNFIAME 80
Cdd:PRK07967 1 MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVKLDPTGLIDRKVMRFMGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 81 QAIKDSGLEATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGSPKRMGPFMVTRCMSSTNSACLATPFKIKGVNYSITS 160
Cdd:PRK07967 81 QAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 161 ACSTSAHCIGNGTELIQMGKQDIVFAGGGEELDWTLSCLFDAMGAMSSKYNDAPETASRPFDATRDGFVIAGGGGVVVLE 240
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTKYNDTPEKASRAYDANRDGFVIAGGGGVVVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 241 ELEHALARGAKIYAEVTGYGATSDGADMVAPSGEGGERSMRLALGTLpeGRRVDYINAHGTSTPAGDVTEVRAIRRIFGE 320
Cdd:PRK07967 241 ELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMALATV--DTPIDYINTHGTSTPVGDVKELGAIREVFGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 321 gKVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREGVEIDSVLSNSFGFGGTNA 400
Cdd:PRK07967 319 -KSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNAELTTVMSNSFGFGGTNA 397
|
....*...
gi 499658371 401 SLLLSKFN 408
Cdd:PRK07967 398 TLVFRRYK 405
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
2-407 |
1.79e-180 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 508.10 E-value: 1.79e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 2 RRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHG-MPDLVLEDHVDKRDLRFMGAGAAYNFIAME 80
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGeVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 81 QAIKDSGLEATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGsPKRMGPFMVTRCMSSTNSACLATPFKIKGVNYSITS 160
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKG-PRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVST 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 161 ACSTSAHCIGNGTELIQMGKQDIVFAGGGE-ELDWTLSCLFDAMGAMSSKyNDAPETASRPFDATRDGFVIAggggvvvl 239
Cdd:COG0304 160 ACASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTR-NDDPEKASRPFDKDRDGFVLGegagvlvl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 240 eeleHALARGAKIYAEVTGYGATSDGADMVA--PSGEGGERSMRLAL---GTLPEgrRVDYINAHGTSTPAGDVTEVRAI 314
Cdd:COG0304 239 eeleHAKARGAKIYAEVVGYGASSDAYHITApaPDGEGAARAMRAALkdaGLSPE--DIDYINAHGTSTPLGDAAETKAI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 315 RRIFGE-GKVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREgVEIDSVLSNSF 393
Cdd:COG0304 317 KRVFGDhAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEARE-AKIDYALSNSF 395
|
410
....*....|....
gi 499658371 394 GFGGTNASLLLSKF 407
Cdd:COG0304 396 GFGGHNASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
2-404 |
3.63e-153 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 438.90 E-value: 3.63e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 2 RRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHG-MPDLVLEDHVDKRDLRFMGAGAAYNFIAME 80
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGeVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 81 QAIKDSGLEATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGsPKRMGPFMVTRCMSSTNSACLATPFKIKGVNYSITS 160
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKG-PRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVST 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 161 ACSTSAHCIGNGTELIQMGKQDIVFAGGGEELDWTLSCL-FDAMGAMSSKYNDaPETASRPFDATRDGFVIAGGGGVVVL 239
Cdd:cd00834 160 ACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAgFAALRALSTRNDD-PEKASRPFDKDRDGFVLGEGAGVLVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 240 EELEHALARGAKIYAEVTGYGATSDGADMVAPS--GEGGERSMRLAL---GTLPEgrRVDYINAHGTSTPAGDVTEVRAI 314
Cdd:cd00834 239 ESLEHAKARGAKIYAEILGYGASSDAYHITAPDpdGEGAARAMRAALadaGLSPE--DIDYINAHGTSTPLNDAAESKAI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 315 RRIFGEG-KVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREgVEIDSVLSNSF 393
Cdd:cd00834 317 KRVFGEHaKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEARE-APIRYALSNSF 395
|
410
....*....|.
gi 499658371 394 GFGGTNASLLL 404
Cdd:cd00834 396 GFGGHNASLVF 406
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
2-404 |
4.55e-129 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 377.60 E-value: 4.55e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 2 RRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHG-MPDLVLEDHVDKRDLRFMGAGAAYNFIAME 80
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGeVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 81 QAIKDSGLEATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGsPKRMGPFMVTRCMSSTNSACLATPFKIKGVNYSITS 160
Cdd:TIGR03150 81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKG-PRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 161 ACSTSAHCIGNGTELIQMGKQDIVFAGGGEEldwTLSCL----FDAMGAMSsKYNDAPETASRPFDATRDGFVIAGGGGV 236
Cdd:TIGR03150 160 ACATGTHAIGDAFRLIQRGDADVMIAGGAEA---AITPLgiagFAAMKALS-TRNDDPEKASRPFDKDRDGFVMGEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 237 VVLEELEHALARGAKIYAEVTGYGATSDGADMVAPS--GEGGERSMRLAL---GTLPEgrRVDYINAHGTSTPAGDVTEV 311
Cdd:TIGR03150 236 LVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPApeGEGAARAMRAALkdaGINPE--DVDYINAHGTSTPLGDKAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 312 RAIRRIFGE-GKVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREgVEIDSVLS 390
Cdd:TIGR03150 314 KAIKKVFGDhAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEARE-AKIDYALS 392
|
410
....*....|....
gi 499658371 391 NSFGFGGTNASLLL 404
Cdd:TIGR03150 393 NSFGFGGTNASLVF 406
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
253-364 |
8.22e-36 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 127.30 E-value: 8.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 253 YAEVTGYGATSDGADMV--APSGEGGERSMRLAL---GTLPEgrRVDYINAHGTSTPAGDVTEVRAIRRIFGEG---KVP 324
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGltAPNGEGQARAIRRALadaGVDPE--DVDYVEAHGTGTPLGDPIEAEALKRVFGSGarkQPL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499658371 325 PISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVT 364
Cdd:pfam02801 79 AIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
156-404 |
5.83e-10 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 60.04 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 156 YSIT--SACSTSAHCIGNGTELIQMGKQDIVFAGGGE-ELDWTLSCLFDAMGAMSskyndaPETASRPFDATRDGFVIAg 232
Cdd:smart00825 89 YSVTvdTACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGe 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 233 gggvvvleeleHALARGAKIYAEVTGYGATSDGAD--MVAPSGEGgersmRLALGtlpegrrvdyinahgtstpagdvte 310
Cdd:smart00825 163 gvgvvvlkrlsDALRDGDPILAVIRGSAVNQDGRSngITAPSGPA-----QLLIG------------------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 311 vrairrifgegkvppisSTKSLTGHSLGATGVheA--IYSILMMQGDFIAASANVTQLDPEIQPDE----IATTLRE--- 381
Cdd:smart00825 213 -----------------SVKSNIGHLEAAAGV--AglIKVVLALKHGVIPPTLHFETPNPHIDLEEsplrVPTELTPwpp 273
|
250 260
....*....|....*....|....*
gi 499658371 382 --GVEIDSVlsNSFGFGGTNASLLL 404
Cdd:smart00825 274 pgRPRRAGV--SSFGFGGTNAHVIL 296
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
1-408 |
0e+00 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 679.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 1 MRRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHGMPDLVLEDHVDKRDLRFMGAGAAYNFIAME 80
Cdd:PRK07967 1 MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVKLDPTGLIDRKVMRFMGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 81 QAIKDSGLEATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGSPKRMGPFMVTRCMSSTNSACLATPFKIKGVNYSITS 160
Cdd:PRK07967 81 QAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 161 ACSTSAHCIGNGTELIQMGKQDIVFAGGGEELDWTLSCLFDAMGAMSSKYNDAPETASRPFDATRDGFVIAGGGGVVVLE 240
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTKYNDTPEKASRAYDANRDGFVIAGGGGVVVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 241 ELEHALARGAKIYAEVTGYGATSDGADMVAPSGEGGERSMRLALGTLpeGRRVDYINAHGTSTPAGDVTEVRAIRRIFGE 320
Cdd:PRK07967 241 ELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMALATV--DTPIDYINTHGTSTPVGDVKELGAIREVFGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 321 gKVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREGVEIDSVLSNSFGFGGTNA 400
Cdd:PRK07967 319 -KSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNAELTTVMSNSFGFGGTNA 397
|
....*...
gi 499658371 401 SLLLSKFN 408
Cdd:PRK07967 398 TLVFRRYK 405
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
2-407 |
1.79e-180 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 508.10 E-value: 1.79e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 2 RRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHG-MPDLVLEDHVDKRDLRFMGAGAAYNFIAME 80
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGeVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 81 QAIKDSGLEATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGsPKRMGPFMVTRCMSSTNSACLATPFKIKGVNYSITS 160
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKG-PRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVST 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 161 ACSTSAHCIGNGTELIQMGKQDIVFAGGGE-ELDWTLSCLFDAMGAMSSKyNDAPETASRPFDATRDGFVIAggggvvvl 239
Cdd:COG0304 160 ACASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTR-NDDPEKASRPFDKDRDGFVLGegagvlvl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 240 eeleHALARGAKIYAEVTGYGATSDGADMVA--PSGEGGERSMRLAL---GTLPEgrRVDYINAHGTSTPAGDVTEVRAI 314
Cdd:COG0304 239 eeleHAKARGAKIYAEVVGYGASSDAYHITApaPDGEGAARAMRAALkdaGLSPE--DIDYINAHGTSTPLGDAAETKAI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 315 RRIFGE-GKVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREgVEIDSVLSNSF 393
Cdd:COG0304 317 KRVFGDhAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEARE-AKIDYALSNSF 395
|
410
....*....|....
gi 499658371 394 GFGGTNASLLLSKF 407
Cdd:COG0304 396 GFGGHNASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
2-404 |
3.63e-153 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 438.90 E-value: 3.63e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 2 RRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHG-MPDLVLEDHVDKRDLRFMGAGAAYNFIAME 80
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGeVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 81 QAIKDSGLEATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGsPKRMGPFMVTRCMSSTNSACLATPFKIKGVNYSITS 160
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKG-PRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVST 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 161 ACSTSAHCIGNGTELIQMGKQDIVFAGGGEELDWTLSCL-FDAMGAMSSKYNDaPETASRPFDATRDGFVIAGGGGVVVL 239
Cdd:cd00834 160 ACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAgFAALRALSTRNDD-PEKASRPFDKDRDGFVLGEGAGVLVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 240 EELEHALARGAKIYAEVTGYGATSDGADMVAPS--GEGGERSMRLAL---GTLPEgrRVDYINAHGTSTPAGDVTEVRAI 314
Cdd:cd00834 239 ESLEHAKARGAKIYAEILGYGASSDAYHITAPDpdGEGAARAMRAALadaGLSPE--DIDYINAHGTSTPLNDAAESKAI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 315 RRIFGEG-KVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREgVEIDSVLSNSF 393
Cdd:cd00834 317 KRVFGEHaKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEARE-APIRYALSNSF 395
|
410
....*....|.
gi 499658371 394 GFGGTNASLLL 404
Cdd:cd00834 396 GFGGHNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
1-407 |
3.35e-130 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 380.67 E-value: 3.35e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 1 MRRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHG-MPDLVLEDHVDKRDLRFMGAGAAYNFIAM 79
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGeVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 80 EQAIKDSGLEATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGsPKRMGPFMVTRCMSSTNSACLATPFKIKGVNYSIT 159
Cdd:PRK07314 81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKG-PRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 160 SACSTSAHCIGNGTELIQMGKQDIVFAGGGEEldwTLSCL----FDAMGAMSSKyNDAPETASRPFDATRDGFVIAGGGG 235
Cdd:PRK07314 160 TACATGAHAIGDAARLIAYGDADVMVAGGAEA---AITPLgiagFAAARALSTR-NDDPERASRPFDKDRDGFVMGEGAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 236 VVVLEELEHALARGAKIYAEVTGYGATSDGADMVAPS--GEGGERSMRLAL---GTLPEgrRVDYINAHGTSTPAGDVTE 310
Cdd:PRK07314 236 ILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPApdGEGAARAMKLALkdaGINPE--DIDYINAHGTSTPAGDKAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 311 VRAIRRIFGEG--KVpPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREGvEIDSV 388
Cdd:PRK07314 314 TQAIKRVFGEHayKV-AVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARER-KIDYA 391
|
410
....*....|....*....
gi 499658371 389 LSNSFGFGGTNASLLLSKF 407
Cdd:PRK07314 392 LSNSFGFGGTNASLVFKRY 410
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
2-404 |
4.55e-129 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 377.60 E-value: 4.55e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 2 RRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHG-MPDLVLEDHVDKRDLRFMGAGAAYNFIAME 80
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGeVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 81 QAIKDSGLEATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGsPKRMGPFMVTRCMSSTNSACLATPFKIKGVNYSITS 160
Cdd:TIGR03150 81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKG-PRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 161 ACSTSAHCIGNGTELIQMGKQDIVFAGGGEEldwTLSCL----FDAMGAMSsKYNDAPETASRPFDATRDGFVIAGGGGV 236
Cdd:TIGR03150 160 ACATGTHAIGDAFRLIQRGDADVMIAGGAEA---AITPLgiagFAAMKALS-TRNDDPEKASRPFDKDRDGFVMGEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 237 VVLEELEHALARGAKIYAEVTGYGATSDGADMVAPS--GEGGERSMRLAL---GTLPEgrRVDYINAHGTSTPAGDVTEV 311
Cdd:TIGR03150 236 LVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPApeGEGAARAMRAALkdaGINPE--DVDYINAHGTSTPLGDKAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 312 RAIRRIFGE-GKVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREgVEIDSVLS 390
Cdd:TIGR03150 314 KAIKKVFGDhAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEARE-AKIDYALS 392
|
410
....*....|....
gi 499658371 391 NSFGFGGTNASLLL 404
Cdd:TIGR03150 393 NSFGFGGTNASLVF 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-407 |
1.09e-101 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 308.47 E-value: 1.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 1 MRRVVITGIGIVSPIGNNAAEVEASLRAGRSGIS-----FSEDYAhhgfrSQIHGM-PDLVL--------EDHVDKRDLR 66
Cdd:PRK06333 3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRtltdfPVGDLA-----TKIGGQvPDLAEdaeagfdpDRYLDPKDQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 67 FMGAGAAYNFIAMEQAIKDSGLEATEVSNP-RTGLVMGSGGPSTSNFFQAHKIVIEKGsPKRMGPFMVTRCMSSTNSACL 145
Cdd:PRK06333 78 KMDRFILFAMAAAKEALAQAGWDPDTLEDReRTATIIGSGVGGFPAIAEAVRTLDSRG-PRRLSPFTIPSFLTNMAAGHV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 146 ATPFKIKGVNYSITSACSTSAHCIGNGTELIQMGKQDIVFAGGGEE--LDWTLSClFDAMGAMSSKYNDAPETASRPFDA 223
Cdd:PRK06333 157 SIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAaiDRVSLAG-FAAARALSTRFNDAPEQASRPFDR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 224 TRDGFVIAGGGGVVVLEELEHALARGAKIYAEVTGYGATSDGADMVAP--SGEGGERSMRLAL---GTLPEgrRVDYINA 298
Cdd:PRK06333 236 DRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGpeDGEGARRAMLIALrqaGIPPE--EVQHLNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 299 HGTSTPAGDVTEVRAIRRIFGEGKVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQP-DEIAT 377
Cdd:PRK06333 314 HATSTPVGDLGEVAAIKKVFGHVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGlDVVAN 393
|
410 420 430
....*....|....*....|....*....|
gi 499658371 378 TLREgVEIDSVLSNSFGFGGTNASLLLSKF 407
Cdd:PRK06333 394 KARP-MDMDYALSNGFGFGGVNASILFRRW 422
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
11-407 |
6.25e-97 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 295.83 E-value: 6.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 11 IVSPIGNNAAEVEASLRAGRSGI-----------SFSEDYAHH-----GFRSQIHGMPDLVLEDHVD----KRDLRFMGA 70
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIrkltefpkflpDCIPEQKALenlvaAMPCQIAAEVDQSEFDPSDfaptKRESRATHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 71 GAAynfiAMEQAIKDSGL-EATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGsPKRMGPFMVTRCMSSTNSACLATPF 149
Cdd:PTZ00050 81 AMA----AAREALADAKLdILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKG-HSRVSPYFIPKILGNMAAGLVAIKH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 150 KIKGVNYSITSACSTSAHCIGNGTELIQMGKQDIVFAGGGEELDWTLSCL-FDAMGAMSSKYNDAPETASRPFDATRDGF 228
Cdd:PTZ00050 156 KLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAgFSRMRALCTKYNDDPQRASRPFDKDRAGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 229 VIAGGGGVVVLEELEHALARGAKIYAEVTGYGATSDGADMVAP--SGEGGERSMRLAL--GTLPEGRRVDYINAHGTSTP 304
Cdd:PTZ00050 236 VMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPhpDGRGARRCMENALkdGANININDVDYVNAHATSTP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 305 AGDVTEVRAIRRIFGEGKVPP--ISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEI-ATTLRE 381
Cdd:PTZ00050 316 IGDKIELKAIKKVFGDSGAPKlyVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVqGKTAHP 395
|
410 420
....*....|....*....|....*.
gi 499658371 382 GVEIDSVLSNSFGFGGTNASLLLSKF 407
Cdd:PTZ00050 396 LQSIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
1-404 |
1.03e-90 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 279.57 E-value: 1.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 1 MRRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHH-GFRSQIHG-MPDLVLEDHVDKRDLRFMGAGAAYNFIA 78
Cdd:PRK09116 1 MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRYdGLNTRLAApIDDFELPAHYTRKKIRSMGRVSLMATRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 79 MEQAIKDSGLEATEV-SNPRTGLVMGSGGPSTSNFfQAHKIVIEKGSPKRMGPFMVTRCMSSTNSACLATPFKIKGVNYS 157
Cdd:PRK09116 81 SELALEDAGLLGDPIlTDGRMGIAYGSSTGSTDPI-GAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKGRVIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 158 ITSACSTSAHCIGNGTELIQMGKQDIVFAGGGEELDWTLSCLFDAMGAMSSKyNDAPETASRPFDATRDGFVIAGGGGVV 237
Cdd:PRK09116 160 TSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTR-NDAPELTPRPFDANRDGLVIGEGAGTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 238 VLEELEHALARGAKIYAEVTGYGATSDGADMVAPSGEGGERSMRLAL---GTLPEgrRVDYINAHGTSTPAGDVTEVRAI 314
Cdd:PRK09116 239 VLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQIAMELALkdaGLAPE--DIGYVNAHGTATDRGDIAESQAT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 315 RRIFGEGKvpPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQP-DEIATTLREgVEIDSVLSNSF 393
Cdd:PRK09116 317 AAVFGARM--PISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGAlDYIMGEARE-IDTEYVMSNNF 393
|
410
....*....|.
gi 499658371 394 GFGGTNASLLL 404
Cdd:PRK09116 394 AFGGINTSLIF 404
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
1-407 |
1.99e-86 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 268.52 E-value: 1.99e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 1 MRRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHGM-----PDLVLEDHVDKRDLRFMGAGAAyn 75
Cdd:PRK08439 1 MKRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEitdfdPTEVMDPKEVKKADRFIQLGLK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 76 fiAMEQAIKDSGLEATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGsPKRMGPFMVTRCMSSTNSACLATPFKIKGVN 155
Cdd:PRK08439 79 --AAREAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKG-PRKISPFFIPSALVNMLGGFISIEHGLKGPN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 156 YSITSACSTSAHCIGNGTELIQMGKQDIVFAGGGEeldwTLSCL-----FDAMGAMSSKyNDAPETASRPFDATRDGFVI 230
Cdd:PRK08439 156 LSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAE----SAICPvgiggFAAMKALSTR-NDDPKKASRPFDKDRDGFVM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 231 AGGGGVVVLEELEHALARGAKIYAEVTGYGATSDGADMVAPSGEGGERSMRLALgTLPEGRRVDYINAHGTSTPAGDVTE 310
Cdd:PRK08439 231 GEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGPLRAMKAAL-EMAGNPKIDYINAHGTSTPYNDKNE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 311 VRAIRRIFG-EGKVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREgVEIDSVL 389
Cdd:PRK08439 310 TAALKELFGsKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARK-AELNVVM 388
|
410
....*....|....*...
gi 499658371 390 SNSFGFGGTNASLLLSKF 407
Cdd:PRK08439 389 SNSFGFGGTNGVVIFKKV 406
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
2-405 |
7.42e-85 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 265.50 E-value: 7.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 2 RRVVITGIGIVSPIGNNAAEVEASLRAGRSGI-----------SFSEDYAHHGFR---SQIHGM-PDLVLEDHVD----- 61
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVraltqddlkmkSEDEETQLYTLDqlpSRVAALvPRGTGPGDFDeelwl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 62 --KRDLRFMGagaaYNFIAMEQAIKDSG-LEATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGSpKRMGPFMVTRCMS 138
Cdd:PLN02836 86 nsRSSSRFIG----YALCAADEALSDARwLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRL-RRLSPFFVPRILI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 139 STNSACLATPFKIKGVNYSITSACSTSAHCIGNGTELIQMGKQDIVFAGGGEELDWTLSCL-FDAMGAMSSKYNDAPETA 217
Cdd:PLN02836 161 NMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAgFSRSRALSTKFNSCPTEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 218 SRPFDATRDGFVIAGGGGVVVLEELEHALARGAKIYAEVTGYGATSDGADMVAPS--GEGGERSMRLAL---GTLPegRR 292
Cdd:PLN02836 241 SRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHedGRGAVLAMTRALqqsGLHP--NQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 293 VDYINAHGTSTPAGDVTEVRAIRRIFGEGKVP---PISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPE 369
Cdd:PLN02836 319 VDYVNAHATSTPLGDAVEARAIKTVFSEHATSgglAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPI 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 499658371 370 IQPDEIATTLREGVEIDSVLSNSFGFGGTNASLLLS 405
Cdd:PLN02836 399 FDDGFVPLTASKAMLIRAALSNSFGFGGTNASLLFT 434
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
2-407 |
4.48e-84 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 262.63 E-value: 4.48e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 2 RRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHGM-PDLVLEDHVDKRDLRFMGAGAAYNFIAME 80
Cdd:PRK08722 4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLvKDFNCEEYMSKKDARKMDLFIQYGIAAGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 81 QAIKDSGLEATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGsPKRMGPFMVTRCMSSTNSACLATPFKIKGVNYSITS 160
Cdd:PRK08722 84 QALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKG-PRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAIST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 161 ACSTSAHCIGNGTELIQMGKQDIVFAGGGEELDWTLSCL-FDAMGAMSSKyNDAPETASRPFDATRDGFVIAGGGGVVVL 239
Cdd:PRK08722 163 ACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAgFGAAKALSTR-NDEPQKASRPWDKDRDGFVLGDGAGMMVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 240 EELEHALARGAKIYAEVTGYGATSDGADMVAPS--GEGGERSMRLALGTLP-EGRRVDYINAHGTSTPAGDVTEVRAIRR 316
Cdd:PRK08722 242 EEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSedGSGGALAMEAAMRDAGvTGEQIGYVNAHGTSTPAGDVAEIKGIKR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 317 IFGE--GKVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREGVEIDSVLSNSFG 394
Cdd:PRK08722 322 ALGEagSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVESMEYAICNSFG 401
|
410
....*....|...
gi 499658371 395 FGGTNASLLLSKF 407
Cdd:PRK08722 402 FGGTNGSLIFKKM 414
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
2-404 |
7.60e-75 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 238.88 E-value: 7.60e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 2 RRVVITGIGIVSPIGNNAAEVEA---SLRAGRSGISFSEDyAHHGFRSQIHGMPDLvleDHVDKRDLRFMGA---GAAYN 75
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDEVEEfweALREGRSGIAPVAR-LKSRFDRGVAGQIPT---GDIPGWDAKRTGIvdrTTLLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 76 FIAMEQAIKDSGLE-ATEVSNPRTGLVMGSGGPSTSnfFQAHKIVIEKgspKRMGPFMVTRCMSSTN--SACLATPFKIK 152
Cdd:cd00828 77 LVATEEALADAGITdPYEVHPSEVGVVVGSGMGGLR--FLRRGGKLDA---RAVNPYVSPKWMLSPNtvAGWVNILLLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 153 -GVNYSITSACSTSAHCIGNGTELIQMGKQDIVFAGGGEELDWTLSCLFDAMGAMSSKYnDAPETASRPFDATRDGFVIA 231
Cdd:cd00828 152 hGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALSTAE-EEPEEMSRPFDETRDGFVEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 232 GGGGVVVLEELEHALARGAKIYAEVTGYGATSDGADMVAPSGEGG-ERSMRLAL-GTLPEGRRVDYINAHGTSTPAGDVT 309
Cdd:cd00828 231 EGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGKGiARAIRTALaKAGLSLDDLDVISAHGTSTPANDVA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 310 EVRAIRRIFGE-GKVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLR-EGVEIDS 387
Cdd:cd00828 311 ESRAIAEVAGAlGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRdLNLKVRA 390
|
410
....*....|....*..
gi 499658371 388 VLSNSFGFGGTNASLLL 404
Cdd:cd00828 391 ALVNAFGFGGSNAALVL 407
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
74-404 |
2.37e-74 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 235.22 E-value: 2.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 74 YNFIAMEQAIKDSGLEATEVSNPRTGLVMGSGGPStsnffqAHKIVIEKGSPKRMGPFMVTRCMSSTNSACLATPFKIKG 153
Cdd:cd00825 14 LGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGS------PRFQVFGADAMRAVGPYVVTKAMFPGASGQIATPLGIHG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 154 VNYSITSACSTSAHCIGNGTELIQMGKQDIVFAGGGEELDWTLSCLFDAMGAMSSkyndaPETASRPFDATRDGFVIAGG 233
Cdd:cd00825 88 PAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST-----PEKASRTFDAAADGFVFGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 234 GGVVVLEELEHALARGAKIYAEVTGYGATSDGADMV--APSGEGGERSMRLAL---GTLPEgrRVDYINAHGTSTPAGDV 308
Cdd:cd00825 163 AGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGafAPSAEGLARAAKEALavaGLTVW--DIDYLVAHGTGTPIGDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 309 TEVRAIRRIFGeGKVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREGveiDSV 388
Cdd:cd00825 241 KELKLLRSEFG-DKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETTPREL---RTA 316
|
330
....*....|....*.
gi 499658371 389 LSNSFGFGGTNASLLL 404
Cdd:cd00825 317 LLNGFGLGGTNATLVL 332
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
2-408 |
4.31e-63 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 211.76 E-value: 4.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 2 RRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHG-----MPDLVLEDHVDKRDLRFMgagaAYNF 76
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGeiksfSTDGWVAPKLSKRMDKFM----LYLL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 77 IAMEQAIKDSGLEA---TEVSNPRTGLVMGSGGPSTSNFFQAhkIVIEKGSPKRMGPFMVTRCMSSTNSACLATPFKIKG 153
Cdd:PLN02787 205 TAGKKALADGGITEdvmKELDKTKCGVLIGSAMGGMKVFNDA--IEALRISYRKMNPFCVPFATTNMGSAMLAMDLGWMG 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 154 VNYSITSACSTSAHCIGNGTELIQMGKQDIVFAGGGEELDWTLSCL-FDAMGAMSSKyNDAPETASRPFDATRDGFVIAG 232
Cdd:PLN02787 283 PNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGgFVACRALSQR-NDDPTKASRPWDMNRDGFVMGE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 233 GGGVVVLEELEHALARGAKIYAEVTGYGATSDGADMVAPSGEGG------ERSMRLAlGTLPEgrRVDYINAHGTSTPAG 306
Cdd:PLN02787 362 GAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAgvilciEKALAQS-GVSKE--DVNYINAHATSTKAG 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 307 DVTEVRAIRRIFGEGKVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREGVEID 386
Cdd:PLN02787 439 DLKEYQALMRCFGQNPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERLDIK 518
|
410 420
....*....|....*....|..
gi 499658371 387 SVLSNSFGFGGTNASLLLSKFN 408
Cdd:PLN02787 519 VALSNSFGFGGHNSSILFAPYK 540
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
1-406 |
7.67e-63 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 207.58 E-value: 7.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 1 MRRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHG---------MPDLVLEDHVDKRDLRFMGAG 71
Cdd:PRK07103 1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPDDAGAGlasafigaeLDSLALPERLDAKLLRRASLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 72 AAYNFIAMEQAIKDSGLEATEVSnpRTGLVMGSggpstSNF-----FQAHKIVIEKgsPKRMGPFMVTRCMSSTNSACLA 146
Cdd:PRK07103 81 AQAALAAAREAWRDAALGPVDPD--RIGLVVGG-----SNLqqreqALVHETYRDR--PAFLRPSYGLSFMDTDLVGLCS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 147 TPFKIKGVNYSITSACSTSAHCIGNGTELIQMGKQDIVFAGGG-EELDWTLSCLFDAMGAM-SSKYNDAPETASRPFDAT 224
Cdd:PRK07103 152 EQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGAlMDLSYWECQALRSLGAMgSDRFADEPEAACRPFDQD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 225 RDGFVIAGGGGVVVLEELEHALARGAKIYAEVTGYGATSDGADMVAPSGEGGERSMRLAL---GTLPEgrRVDYINAHGT 301
Cdd:PRK07103 232 RDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGEMRVIRAALrraGLGPE--DIDYVNPHGT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 302 STPAGDVTEVRAirrIFGEGKVPP-ISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQ-LDPEIQpdeIATTL 379
Cdd:PRK07103 310 GSPLGDETELAA---LFASGLAHAwINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEpIDERFR---WVGST 383
|
410 420
....*....|....*....|....*..
gi 499658371 380 REGVEIDSVLSNSFGFGGTNASLLLSK 406
Cdd:PRK07103 384 AESARIRYALSLSFGFGGINTALVLER 410
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
68-407 |
1.14e-61 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 202.65 E-value: 1.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 68 MGAGAAYNFIAMEQAIKDSglEATEvSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGsPKRMGPFMVTRCMSSTNSACLAT 147
Cdd:PRK14691 1 MGRWWRYKWITFHPSLTHA--DNTE-KQERTATIIGAGIGGFPAIAHAVRTSDSRG-PKRLSPFTVPSFLVNLAAGHVSI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 148 PFKIKGVNYSITSACSTSAHCIGNGTELIQMGKQDIVFAGGGEELDWTLSCL-FDAMGAMSSKYNDAPETASRPFDATRD 226
Cdd:PRK14691 77 KHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAgFAAARALSTHFNSTPEKASRPFDTARD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 227 GFVIAGGGGVVVLEELEHALARGAKIYAEVTGYGATSDGADMV--APSGEGGERSMRLAL---GTLPEgrRVDYINAHGT 301
Cdd:PRK14691 157 GFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTsgAEDGDGAYRAMKIALrqaGITPE--QVQHLNAHAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 302 STPAGDVTEVRAIRRIFGEGKVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLRE 381
Cdd:PRK14691 235 STPVGDLGEINAIKHLFGESNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAGNAQ 314
|
330 340
....*....|....*....|....*.
gi 499658371 382 GVEIDSVLSNSFGFGGTNASLLLSKF 407
Cdd:PRK14691 315 PHDMTYALSNGFGFAGVNASILLKRW 340
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
4-407 |
4.35e-59 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 198.03 E-value: 4.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 4 VVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRS--QIHGMPDLVLEDHVDKRDLRFMGAGAAYNFIAMEQ 81
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEEFDLpvRIGGHLLEEFDHQLTRVELRRMSYLQRMSTVLGRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 82 AIKDSGleATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEKGSpKRMGPFMVTRCMSSTNSACLATPFKIKGVNYSITSA 161
Cdd:PRK07910 94 VWENAG--SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGL-RAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVSA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 162 CSTSAHCIGNGTELIQMGKQDIVFAGGGE-ELDWTLSCLFDAMGAMSSKYNDAPETASRPFDATRDGFVIAGGGGVVVLE 240
Cdd:PRK07910 171 CASGSEAIAQAWRQIVLGEADIAICGGVEtRIEAVPIAGFAQMRIVMSTNNDDPAGACRPFDKDRDGFVFGEGGALMVIE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 241 ELEHALARGAKIYAEVTGYGATSDGADMVA--PSGEGGERSMRLAL---GTLPEGrrVDYINAHGTSTPAGDVTEVRAIR 315
Cdd:PRK07910 251 TEEHAKARGANILARIMGASITSDGFHMVApdPNGERAGHAMTRAIelaGLTPGD--IDHVNAHATGTSVGDVAEGKAIN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 316 RIFGEGKvPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREGvEIDSVLSNSFGF 395
Cdd:PRK07910 329 NALGGHR-PAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPG-NYRYAINNSFGF 406
|
410
....*....|..
gi 499658371 396 GGTNASLLLSKF 407
Cdd:PRK07910 407 GGHNVALAFGRY 418
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
1-406 |
7.32e-55 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 186.20 E-value: 7.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 1 MRRVVITGIGIVSPIGNNAAEVEASLRAGRSG----ISFsEDYAHHGFRSQIHGMPDLVLEDH---VDKRDLRFMGAGAA 73
Cdd:PRK09185 1 MTPVYISAFGATSALGRGLDAILAALRAGRASgmrpCDF-WLVDLPTWVGEVVGVELPALPAAlaaFDCRNNRLALLALQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 74 YNFIAMEQAIKDSGLEatevsnpRTGLVMGSggpSTSNFFQA------------------HKIVIEKGSPkrmgpfmvtr 135
Cdd:PRK09185 80 QIEPAVEAAIARYGAD-------RIGVVLGT---STSGILEGelayrrrdpahgalpadyHYAQQELGSL---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 136 cmsstnSACLATPFKIKGVNYSITSACSTSAHCIGNGTELIQMGKQDIVFAGGGEELdwtlsCL-----FDAMGAMSSky 210
Cdd:PRK09185 140 ------ADFLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSL-----CRltlngFNSLESLSP-- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 211 ndapeTASRPFDATRDGFVIAGGGgvvvleelehALA---RGAKIYAEVTGYGATSDGADMVAP--SGEGGERSMRLAL- 284
Cdd:PRK09185 207 -----QPCRPFSANRDGINIGEAA----------AFFlleREDDAAVALLGVGESSDAHHMSAPhpEGLGAILAMQQALa 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 285 --GTLPEgrRVDYINAHGTSTPAGDVTEVRAIRRIFGEGkvPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASAN 362
Cdd:PRK09185 272 daGLAPA--DIGYINLHGTATPLNDAMESRAVAAVFGDG--VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWN 347
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 499658371 363 VTQLDPEIQPDEIATTlREGVEIDSVLSNSFGFGGTNASLLLSK 406
Cdd:PRK09185 348 TGQPDPALPPLYLVEN-AQALAIRYVLSNSFAFGGNNCSLIFGR 390
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
4-405 |
8.74e-55 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 186.76 E-value: 8.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 4 VVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHGMPDLVLEDHVDKRDLrfmgaGAAYNFIAMEQAI 83
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTVDFLPESPFGASAL-----SEALARLAAEEAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 84 KDSGLEATEVSNP--------------RTGLVMGSGGPSTSNFfqAHKIVIEKGSPKrmgPFMVTRCMSSTNSACLATPF 149
Cdd:PRK06501 88 AQAGIGKGDFPGPlflaappvelewpaRFALAAAVGDNDAPSY--DRLLRAARGGRF---DALHERFQFGSIADRLADRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 150 KIKGVNYSITSACSTSAHCIGNGTELIQMGKQDIVFAGGgeeLDWTLS----CLFDAMGAMSSKyNDAPETASRPFDATR 225
Cdd:PRK06501 163 GTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIA---TDGSVSaealIRFSLLSALSTQ-NDPPEKASKPFSKDR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 226 DGFVIAGGGGVVVLEELEHALARGAKIYAEVTGYGATSDGADMVAPSGEGGE--RSMRLAL---GTLPEGrrVDYINAHG 300
Cdd:PRK06501 239 DGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPaiGAIRAALadaGLTPEQ--IDYINAHG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 301 TSTPAGDVTEVRAIRRIFGEG-KVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTL 379
Cdd:PRK06501 317 TSTPENDKMEYLGLSAVFGERlASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVA 396
|
410 420
....*....|....*....|....*.
gi 499658371 380 REgVEIDSVLSNSFGFGGTNASLLLS 405
Cdd:PRK06501 397 RD-ARVTAVLSNSFGFGGQNASLVLT 421
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
1-406 |
1.15e-45 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 161.76 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 1 MRRVVITGIGIVSPIGNnAAEVEASLRAGRSGISFsedyaHHGFRsQIHGMP-DLVLEDHVDKRDLRFMgagaaynfiAM 79
Cdd:PRK05952 1 MMKVVVTGIGLVSALGD-LEQSWQRLLQGKSGIKL-----HQPFP-ELPPLPlGLIGNQPSSLEDLTKT---------VV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 80 EQAIKDSGLEATEVSnprTGLVMGSggpstSNFFQA---------HKIVIEKGSPKRMGPFMVTrcMSSTNSACLATPFK 150
Cdd:PRK05952 65 TAALKDAGLTPPLTD---CGVVIGS-----SRGCQGqweklarqmYQGDDSPDEELDLENWLDT--LPHQAAIAAARQIG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 151 IKGVNYSITSACSTSAHCIGNGTELIQMGKQDIVFAGGGEELDWTLS-CLFDAMGAMsskyndAPETASrPFDATRDGFV 229
Cdd:PRK05952 135 TQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTlAGFQQMGAL------AKTGAY-PFDRQREGLV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 230 IAGGGGVVVLEELEHALARGAKIYAEVTGYGATSDGADMVAPSGEGgeRSMRLAL-------GTLPEgrRVDYINAHGTS 302
Cdd:PRK05952 208 LGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDG--KSAIAAIqqclarsGLTPE--DIDYIHAHGTA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 303 TPAGDVTEVRAIRRIFGEGkvPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQldPEIQPDEIATTLREG 382
Cdd:PRK05952 284 TRLNDQREANLIQALFPHR--VAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFDLNFVRQAQQSP 359
|
410 420
....*....|....*....|....
gi 499658371 383 VEidSVLSNSFGFGGTNASLLLSK 406
Cdd:PRK05952 360 LQ--NVLCLSFGFGGQNAAIALGK 381
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
3-404 |
3.43e-43 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 155.79 E-value: 3.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 3 RVVITGIGIVSPIGNNAAEVEASLRAGRSGIS------------FSEDYAHHGFRSQIHGMPDlvledHVDKRDLRFMGA 70
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISeipedrwdadgyYPDPGKPGKTYTRRGGFLD-----DVDAFDAAFFGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 71 GAAYnFIAME-----------QAIKDSGLEATEVSNPRTGLVMGSGGPSTSNFFQAHKIVIEkgspkrmgPFMVTRCMSS 139
Cdd:cd00833 77 SPRE-AEAMDpqqrlllevawEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEID--------AYAATGTSRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 140 TNSACLATPFKIKGVNYSITSACSTSAHCIGNGTELIQMGKQDIVFAGGGE-ELDWTLSCLFDAMGAMSskyndaPETAS 218
Cdd:cd00833 148 FLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNlILSPDMFVGFSKAGMLS------PDGRC 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 219 RPFDATRDGFVIAGGGGVVVLEELEHALARGAKIYAEVTGYGATSDGAD--MVAPSGEGGERSMRLAL---GTLPegRRV 293
Cdd:cd00833 222 RPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTkgITAPSGEAQAALIRRAYaraGVDP--SDI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 294 DYINAHGTSTPAGDVTEVRAIRRIFGEGKVP----PISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPE 369
Cdd:cd00833 300 DYVEAHGTGTPLGDPIEVEALAKVFGGSRSAdqplLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPK 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 499658371 370 IQPDE----IATTLRE-----GVEIDSVlsNSFGFGGTNASLLL 404
Cdd:cd00833 380 IDFEEsplrVPTEARPwpapaGPRRAGV--SSFGFGGTNAHVIL 421
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
74-404 |
2.18e-37 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 136.03 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 74 YNFIAMEQAIKDSGLEatevSNPRTGLVMGSGGPSTSnffqahkiviekgspkrmgpfmvtrcmSSTNSACLATPFKIK- 152
Cdd:cd00327 10 LGFEAAEQAIADAGLS----KGPIVGVIVGTTGGSGE---------------------------FSGAAGQLAYHLGISg 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 153 GVNYSITSACSTSAHCIGNGTELIQMGKQDIVFAGGGEEldwtlsclfdamgamsskyndapetasrpfdatrdgFVIAG 232
Cdd:cd00327 59 GPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------FVFGD 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 233 GGGVVVLEELEHALARGAKIYAEVTGYGATSDGADMV-APSGEGGERSMRLALGTLPEGR-RVDYINAHGTSTPAGDVTE 310
Cdd:cd00327 103 GAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVpAVSGEGLARAARKALEGAGLTPsDIDYVEAHGTGTPIGDAVE 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 311 VRAIRRIFGeGKVPPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASanvtqldpeiqpdeiattlreGVEIDSVLS 390
Cdd:cd00327 183 LALGLDPDG-VRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT---------------------PREPRTVLL 240
|
330
....*....|....
gi 499658371 391 NSFGFGGTNASLLL 404
Cdd:cd00327 241 LGFGLGGTNAAVVL 254
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
253-364 |
8.22e-36 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 127.30 E-value: 8.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 253 YAEVTGYGATSDGADMV--APSGEGGERSMRLAL---GTLPEgrRVDYINAHGTSTPAGDVTEVRAIRRIFGEG---KVP 324
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGltAPNGEGQARAIRRALadaGVDPE--DVDYVEAHGTGTPLGDPIEAEALKRVFGSGarkQPL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499658371 325 PISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVT 364
Cdd:pfam02801 79 AIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
2-231 |
2.62e-33 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 125.05 E-value: 2.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 2 RRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSED-----YAHHGFRSQIHGMPDLV------------LEDHVDKRD 64
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPAdrwdpDKLYDPPSRIAGKIYTKwgglddifdfdpLFFGISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 65 LRFMGAGAAYNFIAMEQAIKDSGLEATEVSNPRTGLVMGSGgpstSNFFQAHKIVIEKGSPKRMGPFMVTrCMSSTNSAC 144
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSG----IGDYAALLLLDEDGGPRRGSPFAVG-TMPSVIAGR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 145 LATPFKIKGVNYSITSACSTSAHCIGNGTELIQMGKQDIVFAGGGE-ELDWTLSCLFDAMGAMSSkynDAPETASRPFDa 223
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSP---DGPCKAFDPFA- 231
|
....*...
gi 499658371 224 trDGFVIA 231
Cdd:pfam00109 232 --DGFVRG 237
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
2-404 |
8.69e-31 |
|
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.
Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 121.70 E-value: 8.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 2 RRVVITGIGIVSPIGNNAAEVEASLRAGRSGISFSEDYAHHGFRSQIHG-MPDLVLEDHVDKRDLRFMGAGAAYNFIAME 80
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGeVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 81 QAIKDSGLEATEVSNPRTGLVMGS---GGPSTSNFFQAhkiVIEKGsPKRMGPFMVTRCMSSTNSACLATPFKIKGVNYS 157
Cdd:cd00832 81 WALADAGVDPAALPPYDMGVVTASaagGFEFGQRELQK---LWSKG-PRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 158 ITS-------ACSTSAHCIGNGTELIQMGKQDIVFAGGGeeldWTLSClfdAMGAMSSkyNDAPETASRPFDATRDGFVI 230
Cdd:cd00832 157 VVAeqaggldALAQARRLVRRGTPLVVSGGVDSALCPWG----WVAQL---SSGRLST--SDDPARAYLPFDAAAAGYVP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 231 AGGGGVVVLEELEHALARGAKIYAEVTGYGATSDGADMvAPSGEGGERSMRLAL---GTLPEgrRVDYINAHGTSTPAGD 307
Cdd:cd00832 228 GEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPG-SGRPPGLARAIRLALadaGLTPE--DVDVVFADAAGVPELD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 308 VTEVRAIRRIFGEGKVpPISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEIQPDEIATTLREgVEIDS 387
Cdd:cd00832 305 RAEAAALAAVFGPRGV-PVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRP-AALRT 382
|
410
....*....|....*..
gi 499658371 388 VLSNSFGFGGTNASLLL 404
Cdd:cd00832 383 ALVLARGRGGFNSALVV 399
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
81-404 |
6.31e-26 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 110.73 E-value: 6.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 81 QAIKDSGLEATEVSNPRTGLVMGSGGPSTSNFFQAHkiviekgsPKRMGPFMVTRCMSSTNSACLATPFKIKGVNYSITS 160
Cdd:COG3321 101 EALEDAGYDPESLAGSRTGVFVGASSNDYALLLLAD--------PEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 161 ACSTS--A-H--CigngtELIQMGKQDIVFAGGGeeldwTLSC------LFDAMGAMSskyndaPETASRPFDATRDGFV 229
Cdd:COG3321 173 ACSSSlvAvHlaC-----QSLRSGECDLALAGGV-----NLMLtpesfiLFSKGGMLS------PDGRCRAFDADADGYV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 230 IAggggvvvleelehALARGAKIYAEVTGYGATSDGAD--MVAPSGEGGERSMRLAL---GTLPEgrRVDYINAHGTSTP 304
Cdd:COG3321 237 RGegvgvvvlkrlsdALRDGDRIYAVIRGSAVNQDGRSngLTAPNGPAQAAVIRRALadaGVDPA--TVDYVEAHGTGTP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 305 AGDVTEVRAIRRIFGEGKVP----PISSTKSLTGHSLGATGVheA--IYSILMMQGDFIAASANVTQLDPEIQPDE---- 374
Cdd:COG3321 315 LGDPIEAAALTAAFGQGRPAdqpcAIGSVKSNIGHLEAAAGV--AglIKAVLALRHGVLPPTLHFETPNPHIDFENspfy 392
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 499658371 375 IATTLRE----------GVeidsvlsNSFGFGGTNASLLL 404
Cdd:COG3321 393 VNTELRPwpagggprraGV-------SSFGFGGTNAHVVL 425
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
145-407 |
5.58e-17 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 83.52 E-value: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 145 LATPFKIKGVNYSITSACSTSAHCIGNG-TELIQmGKQDIVFAGGgeeldwtlSCLfDAMGAMSSKYNDAPETAS----R 219
Cdd:TIGR02813 189 IANRFDLGGMNCVVDAACAGSLAAIRMAlSELLE-GRSEMMITGG--------VCT-DNSPFMYMSFSKTPAFTTnediQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 220 PFDATRDGFVIAGGGGVVVLEELEHALARGAKIYAEVTGYGATSDG--ADMVAPSGEGGERSMRLAL---GTLPegRRVD 294
Cdd:TIGR02813 259 PFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGkfKSIYAPRPEGQAKALKRAYddaGFAP--HTCG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 295 YINAHGTSTPAGDVTEVRAIRRIFGEGKVP----PISSTKSLTGHSLGATGVHEAIYSILMMQGDFIAASANVTQLDPEI 370
Cdd:TIGR02813 337 LIEAHGTGTAAGDVAEFGGLVSVFSQDNDQkqhiALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPKL 416
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499658371 371 QPD----------------EIATTLREGVeidsvlsNSFGFGGTNASLLLSKF 407
Cdd:TIGR02813 417 DIEnspfylntetrpwmqrEDGTPRRAGI-------SSFGFGGTNFHMVLEEY 462
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
156-404 |
5.83e-10 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 60.04 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 156 YSIT--SACSTSAHCIGNGTELIQMGKQDIVFAGGGE-ELDWTLSCLFDAMGAMSskyndaPETASRPFDATRDGFVIAg 232
Cdd:smart00825 89 YSVTvdTACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGe 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 233 gggvvvleeleHALARGAKIYAEVTGYGATSDGAD--MVAPSGEGgersmRLALGtlpegrrvdyinahgtstpagdvte 310
Cdd:smart00825 163 gvgvvvlkrlsDALRDGDPILAVIRGSAVNQDGRSngITAPSGPA-----QLLIG------------------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658371 311 vrairrifgegkvppisSTKSLTGHSLGATGVheA--IYSILMMQGDFIAASANVTQLDPEIQPDE----IATTLRE--- 381
Cdd:smart00825 213 -----------------SVKSNIGHLEAAAGV--AglIKVVLALKHGVIPPTLHFETPNPHIDLEEsplrVPTELTPwpp 273
|
250 260
....*....|....*....|....*
gi 499658371 382 --GVEIDSVlsNSFGFGGTNASLLL 404
Cdd:smart00825 274 pgRPRRAGV--SSFGFGGTNAHVIL 296
|
|
| |
